黑料网

Biochemistry; Biology; Bioinformatics; Diagnostics; Preanalytical

Introduction

The use of laboratory diagnostics, which is an important component of clinical decision-making, is just as dangerous as other healthcare treatments. When discussing laboratory errors, the analytical error is frequently addressed. The impact of pre-analytical mistake on overall error and diagnostic precision is significant. As a result, the preanalytical step is critical to laboratory medicine and lab quality in general [1].

Many parts of laboratory diagnostics have been considerably simplified as a result of remarkable advancements in instrument technology, automation, and computer science, and analytical mistakes are no longer the primary factor impacting the reliability and clinical use of laboratory diagnostics. Evidence from previous decades has shown that focusing solely on analytical aspects cannot ensure quality in clinical laboratories. As a result, additional sources of variation, such as pre-analytical errors, should be prioritized for future quality improvements [2].

The pre-analytical phase is far more prone to uncertainties and mishaps, which can have a significant impact on patient care. It has been discovered that the lack of standardized methods for sample collection, including patient preparation, specimen acquisition, handling, and storage, accounts for up to 93% of all errors seen during the entire diagnostic process. Extra-analytical phase errors are more difficult to control. This emphasizes the significance of good laboratory practise and adherence to the new accreditation standards. Adopting appropriate error avoidance techniques, such as process redesign, the use of extra-analytical standards, and increased communication across various clinical departments, is required [3].

Aptamers are often classified as relatively short single-stranded DNA or RNA molecules that bind to a variety of substrates with high affinity and specificity, including small molecules, peptides, proteins, cells, and tissues. Aptamers are frequently referred to as “synthetic antibodies,” but they are easier to obtain, less expensive to create, and more versatile in many ways than antibodies, which has led to the belief that Aptamers would eventually replace antibodies in many applications [4].

Aptamers first appeared in 1990, when two labs-Tuerk and Gold and Ellington and Szostak—independently published the conceptually similar achievement of selecting RNA sequences that bind to specific target molecules, i.e. Aptamers-a term coined two years later. Although the technical procedures were considerably different, both began with highly complicated combinations of synthesized RNA with random sequencesections. As of April 2020, the approach described by Tuerk and Gold, known as “systematic evolution of ligands by exponential enrichment”, had 9100 citations in Google Scholar. The alternate selection approach revealed by Ellington and Szostak has also had a significant influence, as evidenced by 8400 citations in Google Scholar during the same time period [5].

A better measure of the impact of Aptamers after these two seminal publications can be obtained from major scientific publication databases such as PubMed, which contains over 30 million citations for biomedicine, health, and portions of chemical sciences and bioengineering, but not patents. SciFinder, which now has approximately 47 million records kept by Chemical Abstracts Service, contains information on patents and additional chemistry sources. Both of these databases, which overlap in some respects, are freely available and easy to search in a variety of ways. Chart of annual PubMed articles indexed to the term Aptamers from 1992 to 2019, with Aptamers occurring in any field, e.g. title, abstract, text, etc [6].

Material and Methods

In the first stage, the district livestock office got a list of villages in Konya Province where LSD had previously been reported, and then a freshly contaminated farm was identified. The sampled farm was a large farm that freely participated in this study. The farm owner reported a significant decrease in milk output and cattle with fever for more than two days. Infected animals developed skin and mucous membrane sores, lacrimation, nasal discharge, anorexia, reluctance, emaciation, and swollen lymph nodes. Skin lesions were predominantly found on the neck and back.

Some of the cows also had mammary gland and teat lesions. Clinically ill cattle were given nodular skin lesions, swabs, and blood in EDTA. Traumatic jugular venipuncture using vacationer tubes was used to draw blood samples from each animal’s jugular vein. Brown Swiss cattle aged 1 to 3 years were sampled. Whole blood samples were also collected with and without anticoagulant from healthy cattle Brown Swiss and aged between 1 and 3 from a control farm where LSD was not detected. The body temperatures of the control animals were between 38.1°C and 38.5°C, and no sickness was detected on this farm. Cattle had also not recently been immunized against any illness. There were no exterior, blood, or internal parasites in the control cattle. Furthermore, no differences in management practices were observed between the sampled and control farms [7, 8].

Whole blood samples were centrifuged at 3000 rpm for 10 minutes to separate serum and kept at 20°C until testing. Buffy coats were isolated from EDTA blood using PBS containing 2% v/v foetal bovine serum and kept at 20°C until PCR analysis.

Discussion

Lumpy skin disease is a major transboundary cow disease that has lately moved from Africa to Europe. The disease produces significant economic losses, primarily owing to irreversible hide damage, milk production, abortion and infertility, and emaciation and interruption in cattle and product commerce. There is few LSDV-infected cattle serum biochemical references. The measurement and interpretation of the biochemical profile may aid in understanding the disease’s pathophysiology and prognosis. The blood biochemical characteristics of animals exposed to viral infections vary significantly.

Elevated blood cardiac troponin I levels have been linked to myocardial damage after foot-and-mouth disease virus infection. It was announced that low-density lipoprotein is a natural receptor for bovine viral diarrhoea virus, and it was claimed that aberrant accumulation of cholesterol esters might be used to predict vulnerability to prion infection. Changes in serum ALT, AST, and total protein levels were also revealed to be predictive markers of the course of the bovine leukaemia virus infection. Biochemical signs can aid in understanding the progression of the disease. As a result, the purpose of this study was to look into changes in serum enzyme activity in cattle infected with LSDV [9, 10].

In the current investigation, LSDV-infected cattle showed considerably higher AST concentrations and a marginally negligible increase in ALT. The low ALT activity in cattle liver cells explains the modest increase in ALT rate. It has been shown that an increase in AST concentration in the serum is a sensitive biomarker of hepatocyte injury, even if the damage is subclinical, and can be used to track its progression. AST is found in skeletal muscle and muscular heart cells, in addition to hepatocytes. This increase may be connected to the cardiac harm caused by the virus’s presence in the heart. Infected animals had a marginally significant rise in CK-MB. Another cardiac biomarker that has been linked to myocardial injury is CK-MB. However, because a large proportion of the CK-MB enzyme is found in skeletal muscle, it has been claimed that CK-MB is not adequate for identifying myocardial damage. As a result, skeletal muscle injury may raise the absolute activity of the CK-MB fraction in blood. Cardiovascular troponin I measurement would have aided in the detection of myocardial damage.

Regrettably, this was not done in this study. LSD lesions can develop in both the muscle fascia and the muscle itself. Increased AST levels in sick cattle have also been linked to muscular injury [11].

ALP is an enzyme found in the cells that line the bile ducts of the liver, and its concentration rises with biliary illness, intrahepatic cholestasis, and liver infiltrative disease. We found a considerable rise in ALP concentrations in infected cattle, which contradict prior research that found no change in ALP concentrations in LSDV-infected cattle. The variations between our results and previous ones could be attributed to the stage of the infection and the age of the animals. Both ALP and GGT levels have been observed to be increased in cholestasis. There were no significant GGT changes between the infected and control groups in this investigation. As a result, the increase in AST, ALT, and ALP levels in LSDV-infected cattle can be attributed to the hepatic damage caused by the virus’s presence in the liver. This finding is consistent with prior research that found pox lesions in the liver [12].

An increase in creatinine concentration has been linked to a decrease in glomerular filtration rate. Creatinine levels in the blood were substantially greater in the LSDV-infected group than in the control group. On the contrary, Abu tarbush discovered low creatinine levels in naturally infected LSDV animals. Possible explanations for this variation include sample time, serum biochemical assay methodologies, and individual variability. Absolute muscle mass and level of physical activity has been shown to influence the rate of creatinine generation and thus serum levels. There has also been research on the impact of age, breed, gender, diet, heat stress, lactation, and pregnant period on blood creatinine levels. Whereas the cattle used in Abu tarbush’s study were Holstein-Friesian and ranged in age from 5 months to 10 years. Changes in creatinine concentration between these two trials can also be accounted by changes in cattle muscle mass, nutrition, and physical activity [13].

The current investigation found that total serum protein contents in calves positive for LSD were substantially greater than those in healthy cattle. Furthermore, infected cattle had a marginally significant rise in albumin. This is to be expected because it signifies that the immune system has been activated following infection. Changes in total protein and albumin concentrations have been linked to humoral immune response to infectious microorganisms.

BUN concentrations were found to be higher in LSDV-infected cattle in this study. Albumin concentrations increased somewhat in sick cattle, as did BUN. This can be explained by cow dehydration. Clinical indications of LSDV infection in cattle include fever, anorexia, and lethargy. As a result, dehydration can occur following the onset of LSD’s clinical indications [14-17].

Conclusion

There is a scarcity of published data on the serum biochemistry of LSDV-infected cattle. Blood biochemistry tests indicate that LSD causes liver and kidney damage in cattle. This study contributed to a better knowledge of the disease’s aetiology, and the study’s findings may provide additional insight into improving treatment techniques for LSDV infection.

Conflict of Interest

None

Acknowledgement

None

1. Berardinelli W (1954) . J Clin Endocr 142: 193-204.

, ,

2. Magré J, Delépine M, Khallouf E (2001) . Nat Genet 28: 365-370.

, ,

3. Windpassinger C, Auer-Grumbach M (2004) . Nat Genet 36: 271-276.

, ,

4. Ito D, Fujisawa T, Iida H (2008) Characterization of seipin/BSCL2, . Neurobiol Dis 31: 266-277.

, ,

5. Liu X, Xie B, Qi Y (2016) . Brain Struct Funct 221: 4111-4127.

, ,

6. Uhlen M, Oksvold P, Fagerberg L (2010) . Nat Biotechnol 28: 1248-1250.

, ,

7.  Yu RK, Tsai YT, Yanagisawa M (2011) . J Oleo Sci 60: 537-544.

, ,

8. Schauer R (2004) . Zool 107: 49-64.

, ,

9. Angata T, Varki A (2002) . Chem Rev 102: 439-469.

, ,

10. Schauer R (2009) . Curr Opin Struct Biol 19: 507-514.

, ,

11. Garg AK (2003) . Trends Endocrinol Metab 14: 214-221.

, ,

12. Leung W (2001) . Front Biosci 6: 944-953.

, ,

13. Hall IE, Yarlagadda SG, Coca SG (2010) . Am J Nephrol 21: 189-197.

, ,

14. Jia HM, Huang LF, Zheng Y, Li WX (2017) Crit Care 21: 77.

, ,

15. Bargnoux AS, Piéroni L, Cristol JP (2013) Clin Chem Lab Med 51: 293-296.

, ,

16. Jiang M, Gao M, Wu C (2014) Proc Natl Acad Sci 111: 7054-7059.

, ,

17. Han WK, Bailly V, Abichandani R, Thadhani R,  Bonventre JV, et al. (2002) Kidney Int 62: 237-244.

, ,